The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells

A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis

Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664

Biochemistry of nitric oxide and its redox-activated forms

Stamler, J. S., Singel, D. J., & Loscalzo, J. (1992) · Science · doi:10.1126/science.1281928 · Cited by 2,744

A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds

Lipton, S. A., Choi, Y.-B., Pan, Z.-H., Lei, S. Z., Chen, H.-S. V., Sucher, N. J., Loscalzo, J., Singel, D. J., & Stamler, J. S. (1993) · Nature · doi:10.1038/364626a0 · Cited by 2,433

Macrophage cytotoxicity: role for L-arginine deiminase and imino nitrogen oxidation to nitrite

Hibbs, J. B., Taintor, R. R., & Vavrin, Z. (1987) · Science · doi:10.1126/science.2432665 · Cited by 1,527

Regulating the fate of mRNA: the control of cellular iron metabolism

Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210

Transferrin receptor on endothelium of brain capillaries

Jefferies, W. A., Brandon, M. R., Hunt, S. V., Williams, A. F., Gatter, K. C., & Mason, D. Y. (1984) · Nature · doi:10.1038/312162a0 · Cited by 1,061

Lactoferrin: molecular structure and biological function

Lönnerdal, B., & Iyer, S. (1995) · Annual Review of Nutrition · doi:10.1146/annurev.nu.15.070195.000521 · Cited by 781

Evolution of the first metabolic cycles.

Wächtershäuser, G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.200 · Cited by 751

Iron-Responsive Elements: Regulatory RNA Sequences That Control mRNA Levels and Translation

Casey, J. L., Hentze, M. W., Koeller, D. M., Caughman, S. W., Rouault, T. A., Klausner, R. D., & Harford, J. B. (1988) · Science · doi:10.1126/science.2452485 · Cited by 709

Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin.

Sutherland, R., Delia, D., Schneider, C., Newman, R., Kemshead, J., & Greaves, M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4515 · Cited by 685

Oxidative Stress: Harms and Benefits for Human Health

Pizzino, G., Irrera, N., Cucinotta, M., Pallio, G., Mannino, F., Arcoraci, V., Squadrito, F., Altavilla, D., & Bitto, A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8416763 · Cited by 4,837

Nitric oxide donors: chemical activities and biological applications

Wang, P. G., Xian, M., Tang, X., Wu, X., Wen, Z., Cai, T., & Janczuk, A. J. (2002) · Chemical Reviews · doi:10.1021/cr000040l · Cited by 1,337

The labile iron pool: characterization, measurement, and participation in cellular processes1 1This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.

Kakhlon, O., & Cabantchik, Z. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01006-7 · Cited by 839

The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer

Kalinowski, D. S., & Richardson, D. R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.2 · Cited by 721

Structure of the human transferrin receptor-transferrin complex

Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571

The role of iron in cell cycle progression and the proliferation of neoplastic cells

Le, N. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00068-9 · Cited by 453

Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron.

Canonne-Hergaux, F., Gruenheid, S., Ponka, P., & Gros, P. (1999) · Blood · doi:10.1182/blood.v93.12.4406 · Cited by 451

Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease

Lane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399

Crystal Structure at 2.8 Å of an FcRn/Heterodimeric Fc Complex

Martin, W. L., West, A. P., Gan, L., & Bjorkman, P. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00230-1 · Cited by 391

Identification of a hypoxia response element in the transferrin receptor gene

Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380

Crystal Structure of the Ectodomain of Human Transferrin Receptor

Lawrence, C. M., Ray, S., Babyonyshev, M., Galluser, R., Borhani, D. W., & Harrison, S. C. (1999) · Science · doi:10.1126/science.286.5440.779 · Cited by 315

Mechanisms of Brain Iron Transport: Insight into Neurodegeneration and CNS Disorders

Mills, E., Dong, X.-P., Wang, F., & Xu, H. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.09.140 · Cited by 309

Comparison of the Interactions of Transferrin Receptor and Transferrin Receptor 2 with Transferrin and the Hereditary Hemochromatosis Protein HFE

West, A. P., Bennett, M. J., Sellers, V. M., Andrews, N. C., Enns, C. A., & Bjorkman, P. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000664200 · Cited by 257

Oxidative Stress and the Homeodynamics of Iron Metabolism

Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247

Synthetic and natural iron chelators: Therapeutic potential and clinical use

Hatcher, H. C., Singh, R. N., Torti, F. M., & Torti, S. V. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.121 · Cited by 242

Transferrin receptor (CD71) is a marker of poor prognosis in breast cancer and can predict response to tamoxifen

Habashy, H. O., Powe, D. G., Staka, C. M., Rakha, E. A., Ball, G., Green, A. R., Aleskandarany, M., Paish, E. C., Douglas Macmillan, R., Nicholson, R. I., et al. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0345-x · Cited by 236

The Role of Iron in Neurodegeneration: Prospects for Pharmacotherapy of Parkinson??s Disease

Jellinger, K. A. (1999) · Drugs & Aging · doi:10.2165/00002512-199914020-00004 · Cited by 218

The iron metabolism of neoplastic cells: Alterations that facilitate proliferation?

Kwok, J. C., & Richardson, D. R. (2002) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(01)00213-x · Cited by 215

Macrophages and iron trafficking at the birth and death of red cells

Korolnek, T., & Hamza, I. (2015) · Blood · doi:10.1182/blood-2014-12-567776 · Cited by 196

Chelators at the cancer coalface: Desferrioxamine to Triapine and beyond

Yu, Y., Wong, J., Lovejoy, D. B., Kalinowski, D. S., & Richardson, D. R. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1954 · Cited by 195

Transferrin therapy ameliorates disease in β-thalassemic mice

Li, H., Rybicki, A. C., Suzuka, S. M., von Bonsdorff, L., Breuer, W., Hall, C. B., Cabantchik, Z. I., Bouhassira, E. E., Fabry, M. E., & Ginzburg, Y. Z. (2010) · Nature Medicine · doi:10.1038/nm.2073 · Cited by 192

The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor 1 1Edited by I. A. Wilson

Lebrón, J. A., West, A. P., & Bjorkman, P. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3252 · Cited by 182

Cell Biology of Heme

PONKA, P. (1999) · The American Journal of the Medical Sciences · doi:10.1097/00000441-199910000-00004 · Cited by 182

Iron export through the transporter ferroportin 1 is modulated by the iron chaperone PCBP2

Yanatori, I., Richardson, D. R., Imada, K., & Kishi, F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721936 · Cited by 170

Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mkmice

Canonne-Hergaux, F., Zhang, A.-S., Ponka, P., & Gros, P. (2001) · Blood · doi:10.1182/blood.v98.13.3823 · Cited by 169

Iron and carcinogenesis: from Fenton reaction to target genes

Toyokuni, S. (2002) · Redox Report · doi:10.1179/135100002125000596 · Cited by 166

CD63 is regulated by iron via the IRE-IRP system and is important for ferritin secretion by extracellular vesicles

Yanatori, I., Richardson, D. R., Dhekne, H. S., Toyokuni, S., & Kishi, F. (2021) · Blood · doi:10.1182/blood.2021010995 · Cited by 148

Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: early mRNA induction by haem, followed by iron-dependent protein expression

Delaby, C., Pilard, N., Puy, H., & Canonne-Hergaux, F. (2008) · Biochemical Journal · doi:10.1042/bj20071474 · Cited by 144

Neurodegeneration with brain iron accumulation–clinical syndromes and neuroimaging

Schipper, H. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.06.016 · Cited by 141

Regulation of Vascular Endothelial Growth Factor Synthesis by Nitric Oxide: Facts and Controversies

Dulak, J., & Józkowicz, A. (2003) · Antioxidants & Redox Signaling · doi:10.1089/152308603321223612 · Cited by 130

JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress

Tsuji, Y. (2005) · Oncogene · doi:10.1038/sj.onc.1208901 · Cited by 121

Iron: A New Target for Pharmacological Intervention in Neurodegenerative Diseases

Whitnall, M., & Richardson, D. R. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.008 · Cited by 113

Desferoxamine (DFO)—Mediated iron chelation: Rationale for a novel approach to therapy for brain cancer

Dayani, P. N., Bishop, M. C., Black, K., & Zeltzer, P. M. (2004) · Journal of Neuro-Oncology · doi:10.1023/b:neon.0000024238.21349.37 · Cited by 114

Transferrin and the transferrin receptor for the targeted delivery of therapeutic agents to the brain and cancer cells

Dufès, C., Al Robaian, M., & Somani, S. (2013) · Therapeutic Delivery · doi:10.4155/tde.13.21 · Cited by 110

Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease

Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103

Compartmentalization of iron between mitochondria and the cytosol and its regulation

Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95

Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human macrophages

Olakanmi, O., Schlesinger, L. S., & Britigan, B. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0606405 · Cited by 88

A calorie-restricted diet decreases brain iron accumulation and preserves motor performance in old rhesus monkeys

Kastman, E. K., Willette, A. A., Coe, C. L., Bendlin, B. B., Kosmatka, K. J., McLaren, D. G., Xu, G., Canu, E., Field, A. S., Alexander, A. L., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0835-10.2010 · Cited by 85

Iron, oxidative stress and the example of solar ultraviolet a radiation.

Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74

Disruption of ferroportin 1 regulation causes dynamic alterations in iron homeostasis and erythropoiesis in polycythaemia mice

Mok, H., Jelinek, J., Pai, S., Cattanach, B. M., Prchal, J. T., Youssoufian, H., & Schumacher, A. (2004) · Development · doi:10.1242/dev.01081 · Cited by 73

Frataxin: its role in iron metabolism and the pathogenesis of Friedreich's ataxia

Becker, E., & Richardson, D. R. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00067-4 · Cited by 71

A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin

DUBLJEVIC, V., SALI, A., & GODING, J. W. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3410011 · Cited by 63

The hmuQ and hmuD Genes from Bradyrhizobium japonicum Encode Heme-Degrading Enzymes

Puri, S., & O'Brian, M. R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00737-06 · Cited by 59

Mechanism of cell death by 5-aminolevulinic acid-based photodynamic action and its enhancement by ferrochelatase inhibitors in human histiocytic lymphoma cell line U937

Amo, T., Kawanishi, N., Uchida, M., Fujita, H., Oyanagi, E., Utsumi, T., Ogino, T., Inoue, K., Shuin, T., Utsumi, K., et al. (2009) · Cell Biochemistry and Function · doi:10.1002/cbf.1603 · Cited by 56

Lipophilicity of analogs of pyridoxal isonicotinoyl hydrazone (PIH) determines the efflux of iron complexes and toxicity in K562 cells

Buss, J. L., Arduini, E., Shephard, K. C., & Ponka, P. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01551-4 · Cited by 41

A Calorie-Restricted Diet Decreases Brain Iron Accumulation and Preserves Motor Performance in Old Rhesus Monkeys

Kastman, E. K., Willette, A. A., Coe, C. L., Bendlin, B. B., Kosmatka, K. J., McLaren, D. G., Xu, G., Canu, E., Field, A. S., Alexander, A. L., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.2553-12.2012 · Cited by 40

Therapeutic Potential of Iron Chelators in Cancer Therapy

Richardson, D. R. (2002) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4615-0593-8_12 · Cited by 40

Air pollutants disrupt iron homeostasis to impact oxidant generation, biological effects, and tissue injury

Ghio, A. J., Soukup, J. M., Dailey, L. A., & Madden, M. C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.007 · Cited by 39

A Nitric Oxide Storage and Transport System That Protects Activated Macrophages from Endogenous Nitric Oxide Cytotoxicity

Lok, H. C., Sahni, S., Jansson, P. J., Kovacevic, Z., Hawkins, C. L., & Richardson, D. R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.763714 · Cited by 36

Iron Chelators with Topoisomerase-Inhibitory Activity and Their Anticancer Applications

Rao, V. A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4877 · Cited by 37

Transferrin receptor-1 and 2 expression in chronic lymphocytic leukemia

Smilevska, T., Stamatopoulos, K., Samara, M., Belessi, C., Tsompanakou, A., Paterakis, G., Stavroyianni, N., Athanasiadou, I., Chiotoglou, I., Hadzidimitriou, A., et al. (2006) · Leukemia Research · doi:10.1016/j.leukres.2005.06.006 · Cited by 34